
Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Question
Chapter 26, Problem 9P
Interpretation Introduction
To write:
The chemical mechanisms for 6, 8, 9 steps of the purine biosynthesis.
Concept Introduction:
The purine is an
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Examine the pairs of molecules and identify the more-reduced molecule in each pair.
H-C-
CH,
OH
CH
HO-C-H
CH₁₂
Pyruvate
Ethanol
Acetaldehyde
Lactate
COO
H-C H
H- -C-H
COO-
Succinate
Fumarate
-OOC
COO
H
COO-
H――000-
CH₂
COO-
Oxalosuccinate
H-C-OH
OOC-C-H
CH₂
COO
Isocitrate
Classify each description as characterizing facilitated diffusion, primary active transport, secondary active transport, or both
primary and secondary active transport.
Facilitated diffusion
Primary active transport Secondary active transport
Primary and secondary
active transport
Answer Bank
requires ATP
includes lactose permease
directly uses ATP hydrolysis to pump substances across the membrane
includes the Na+-K+ ATPase pump
always moves more than one substance at a time
movement of substances against an electrochemical gradient
does not require energy input
includes uniporters
uses energy stored in electrochemical gradients generated by pumps
Creatine is a popular dietary supplement.
What is the biochemical rationale for the use of creatine?
It would directly serve as an electron carrier to support the oxidation of fuel molecules and thus energy production.
It would serve as an electron donor to support reductive biosyntheses required to sustain cellular function.
It would be converted into creatine phosphate and thus serve as a rapid means of replenishing ATP during
muscle contraction.
It would promote the movement of ions through ion channels and thus power the synthesis of ATP during exercise.
What type of exercise would benefit most from creatine supplementation?
a leisurely walk
sprinting
yoga
a long-distance run
Chapter 26 Solutions
Biochemistry
Ch. 26 - Prob. 1PCh. 26 - Prob. 2PCh. 26 - Allosteric Regulation of Purine and Pyrimidine...Ch. 26 - Inhibition of Purine and Pyrimidine Metabolism by...Ch. 26 - Prob. 5PCh. 26 - Allosteric Regulation of Ribonucleotide Reductase...Ch. 26 - Prob. 7PCh. 26 - Prob. 8PCh. 26 - Prob. 9PCh. 26 - Prob. 10P
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- Assign each statement to the corresponding polysaccharide. Chitin Starch Glycogen Cellulose Answer Bank is abundant in muscle and liver provides structural support for plants is the storage form of glucose in animals provides structural support for animals such as arthropods is a storage form of fuel in plant cells consists of N-acetylglucosamine residues comes in two forms: amylose and amylopectinarrow_forwardMatch each term with its description. has the molecular formula of (CHO), monosaccharides that differ at a single asymmetric carbon atom the storage form of glucose in animals the storage form of glucose in plants glycoprotein containing glycosaminoglycans the most abundant organic molecule in the biosphere N-acetylgalactosamine is a key component of this glycoprotein carbohydrate-binding proteins enzymes that synthesize oligosaccharides stereoisomers that are mirror images of each other Answer Bank lectins epimers starch mucoprotein carbohydrates glycogen glycosyltransferases cellulose enantiomers proteoglycanarrow_forwardComplete the sentences describing membrane lipids by moving the names of the lipids to the appropriate sentence. Some lipids will be used more than once, and some sentences will require you to place two or three lipids. Answer Bank include two fatty acids joined to glycerol by ester linkages. do not contain glycerol. is a steroid. contain a sphingosine backbone. contain one or more sugars. usually have branched alkyl chains. glycolipids phosphoglycerides sphingomyelin cholesterol archacal lipidsarrow_forward
- The protein content of most plasma membranes is, on average, about 50% by weight. Myelin has a protein content of about 18%, whereas the internal membranes of mitochondria and chloroplasts may be composed of 75% protein. Label the membrane proteins on the diagram. Answer Bank lipid-anchored protein peripheral membrane protein integral membrane proteinarrow_forwardWhy don’t we see amino acids with certain properties (e.g., a straight-chain side chain with two carbons, multiple hydroxyl groups, or other unusual structures)?arrow_forwardPlease analze the gel electrophoresis column of the VRK1 kinase (MW: 39.71 kDa). Lane 1: buffer Lane 2 : Ladder Lane 3: Lysate Lane 4: Flowthrough Lane 5: Wash Lanes 6-8: E1, E2, E3 Lane 9: Dialyzed VRK1 Lane 10: LDHarrow_forward
- Please helparrow_forwardYou have isolated a protein and determined that the native molecular weight of the holoenzyme is 160 kD using size exclusion chromatography. Analysis of this protein using SDS-PAGE revealed 2 bands, one at 100 kD and one at 30 kD. Describe the architecture of the polypeptide component of this enzyme.arrow_forwardIn a cell free preparation of beta-lactamase, penicillin is hydrolyzed in a D2O enriched assay. After one round of catalysis, where would you anticipate finding Deuterium? please help thank youarrow_forward
- To map the active site of -lactamase, the enzyme was hydrolyzed with trypsin to yield a hexapeptide (P1) with the following amino acids. Glu, Lys, Leu, Phe, Met, and Ser. Treatment of P1 with phenyl isothiocyanate yielded a PTH derivative of phenylalanine and a peptide (P2). Treatment of P1 with cyanogenbromide gave an acidic tetrapeptide (P3) and a dipeptide (P4).Treatment of P2 with 1-fluoro-2,4-dinitrobenzene, followed by complete hydrolysis, yields N-2,4-dinitrophenyl-Glu. P1, P2, and P3 contain the active site serine. question: the b-lactamase hydrolyzes the lactam-ring in antibiotics like penicillin. Describe the mechanism, of hydrolysis, insuring to include the involvement of S, D, and K in the reaction sequence. Please help!arrow_forwardThree of these amino acids participate in the proteolytic hydrolysis of polypeptides. Show the charge-relay network generated by the serine proteases and identify the nucleophilic species that initiates the hydrolysis. please help!arrow_forwardYou have isolated a protein and determined that the native molecular weight of the holoenzyme is 160 kD using size exclusion chromatography. Analysis of this protein using SDS-PAGE revealed 2 bands, one at 100 kD and one at 30 kD. 1. Describe the architecture of the polypeptide component of this enzyme. 2. The enzyme was found to be 0.829% NAD (by weight). What further can be said regarding the architecture? can you please help me with question number 2arrow_forward
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